Abstract

The μ opioid receptor (μOR), which is part of the G protein-coupled receptors family, is a membrane protein that is modulated by its lipid environment. In the present work, we model μOR in three different membrane systems: POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine), POPE (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine), and DPPC (1, 2-dipalmitoyl-sn-glycero-3-phosphocholine) through 45 μs molecular dynamics (MD) simulations at the coarse-grained level. Our theoretical studies provide new insights to the lipid-induced modulation of the receptor. Particularly, to characterize how μOR interacts with each lipid, we analyze the tilt of the protein, the number of contacts occurring between the lipids and each amino acid of the receptor, and the μOR-lipid interface described as a network graph. We also analyze the variations in the number and the nature of the protein contacts that are induced by the lipid structure. We show that POPC interacts preferentially
with helix 1 (H1) and helices H5-H6, POPE, with H5-H6 and H6-H7, and DPPC, with H4 and
H6. We demonstrate how each of the three lipids shape the structure of the μOR.
Original languageEnglish
Article numbere0213646
Pages (from-to)e0213646
Number of pages19
JournalPLoS ONE
Volume14
Issue number3
DOIs
Publication statusPublished - 1 Mar 2019

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molecular dynamics
narcotics
Opioid Receptors
Molecular Dynamics Simulation
Molecular dynamics
Lipids
receptors
lipids
Amino Acid Receptors
G-Protein-Coupled Receptors
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine
1-palmitoyl-2-oleoylphosphatidylcholine
colfosceril palmitate
phosphorylethanolamine
membrane proteins
Membrane Proteins
Proteins
Theoretical Models
proteins
Modulation

Cite this

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title = "Interaction of POPC, DPPC, and POPE with the μ opioid receptor: A coarse-grained molecular dynamics study",
abstract = "The μ opioid receptor (μOR), which is part of the G protein-coupled receptors family, is a membrane protein that is modulated by its lipid environment. In the present work, we model μOR in three different membrane systems: POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine), POPE (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine), and DPPC (1, 2-dipalmitoyl-sn-glycero-3-phosphocholine) through 45 μs molecular dynamics (MD) simulations at the coarse-grained level. Our theoretical studies provide new insights to the lipid-induced modulation of the receptor. Particularly, to characterize how μOR interacts with each lipid, we analyze the tilt of the protein, the number of contacts occurring between the lipids and each amino acid of the receptor, and the μOR-lipid interface described as a network graph. We also analyze the variations in the number and the nature of the protein contacts that are induced by the lipid structure. We show that POPC interacts preferentiallywith helix 1 (H1) and helices H5-H6, POPE, with H5-H6 and H6-H7, and DPPC, with H4 andH6. We demonstrate how each of the three lipids shape the structure of the μOR.",
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Interaction of POPC, DPPC, and POPE with the μ opioid receptor : A coarse-grained molecular dynamics study. / Angladon, M-A; Fossépré, Mathieu; Leherte, Laurence; Vercauteren, Daniel.

In: PLoS ONE, Vol. 14, No. 3, e0213646, 01.03.2019, p. e0213646.

Research output: Contribution to journalArticle

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